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Database: UniProt
Entry: F9YR81_CAPCC
LinkDB: F9YR81_CAPCC
Original site: F9YR81_CAPCC 
ID   F9YR81_CAPCC            Unreviewed;       860 AA.
AC   F9YR81;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Ccan_03170 {ECO:0000313|EMBL:AEK22439.1};
OS   Capnocytophaga canimorsus (strain 5).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK22439.1, ECO:0000313|Proteomes:UP000008895};
RN   [1] {ECO:0000313|EMBL:AEK22439.1, ECO:0000313|Proteomes:UP000008895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX   PubMed=21914877; DOI=10.1128/JB.05853-11;
RA   Manfredi P., Pagni M., Cornelis G.R.;
RT   "Complete genome sequence of the dog commensal and human pathogen
RT   Capnocytophaga canimorsus strain 5.";
RL   J. Bacteriol. 193:5558-5559(2011).
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP002113; AEK22439.1; -; Genomic_DNA.
DR   RefSeq; WP_013996434.1; NC_015846.1.
DR   AlphaFoldDB; F9YR81; -.
DR   STRING; 860228.Ccan_03170; -.
DR   KEGG; ccm:Ccan_03170; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_10; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000008895; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW   Hydrolase {ECO:0000313|EMBL:AEK22439.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008895};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          410..521
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   860 AA;  97298 MW;  F05A87AB343AE232 CRC64;
     MNFNNYTIKS QEVVQRAQQI AQSYGHQELQ NEHFFKAIEE VDQNVLPFLL KKLNINREQL
     SKVLETALQS FPKVSGGQMS LSREANTMLN EAVNIAKKMN DEYVSIEHLI LAIFKSNSKI
     GQALKDQGVK EKDLEKAIQE LRKGERVTSA SAEETYNSLN KYAKNLNQMA DSGKLDPVIG
     RDEEIRRVLQ ILSRRTKNNP MLVGEPGVGK TAIAEGLAHR IVQGDVPENL KDKSIYSLDM
     GALIAGAKYK GEFEERLKSV VKEVTSSDGN IILFIDEIHT LVGAGGGEGA MDAANILKPA
     LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVMVEEPD TESAISILRG IKEKYETHHK
     VRIKDEAIIA AVELSERYIT NRFLPDKAID LMDEAAAKLR MEINSKPEEL DVLDRKIMQL
     EIEIEAIKRE NDEQKLKMLY ADVANLKEER NAIFAKWQSE KNVIDEVQTT KEAIENYKLE
     AEKAEREGDY AKVAELRYGK IKEAQDNLVL LQEKLDQAQG NSLIKEEVTS ENIAEVVAKW
     TGIPVTKMLQ GEREKLLKLE SELHKRVVGQ EEAIEAISDA IRRSKAGLQD PKKPIGSFLF
     LGTTGVGKTE LAKALAEYLF DDENAMTRID MSEYQERHAV SRLVGAPPGY VGYDEGGQLT
     EAVRRRPYSV ILLDEIEKAH PDTFNILLQV LDEGRLTDNK GRTADFKNTI IIMTSNIGSH
     LIQESFEKYT NDLEKATEVA KDDVLQLLKQ TVRPEFINRI DDIVMFTPLS RENIRSIVRL
     QLRSIIKMVA RENILLDATD QAIDYLAEKG FDPQFGARPV KRTLQKEVLN RLSKEILSGN
     IHKDKTILLD TFDNQLVFRN
//
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